Structure of PDB 2wtv Chain B

Receptor sequence
>2wtvB (length=264) Species: 9606 (Homo sapiens) [Search protein sequence]
RQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVE
HQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPRGEVYKELQKL
SKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADF
GWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVG
KPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLR
EVLEHPWITANSSK
3D structure
PDB2wtv Crystal Structure of an Aurora-A Mutant that Mimics Aurora-B Bound to Mln8054: Insights Into Selectivity and Drug Design.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D256 K258 E260 N261 D274 T292
Catalytic site (residue number reindexed from 1) D131 K133 E135 N136 D149 T167
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZZL B L139 K141 V147 K162 Y212 A213 G216 L263 A273 D274 V279 L14 K16 V22 K37 Y87 A88 G91 L138 A148 D149 V154 MOAD: Ki=1.8nM
BindingDB: IC50=34nM,Kd=6.5nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0000212 meiotic spindle organization
GO:0000226 microtubule cytoskeleton organization
GO:0000278 mitotic cell cycle
GO:0006468 protein phosphorylation
GO:0007052 mitotic spindle organization
GO:0007098 centrosome cycle
GO:0007100 mitotic centrosome separation
GO:0051321 meiotic cell cycle

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2wtv, PDBe:2wtv, PDBj:2wtv
PDBsum2wtv
PubMed20067443
UniProtO14965|AURKA_HUMAN Aurora kinase A (Gene Name=AURKA)

[Back to BioLiP]